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Information on EC 2.6.1.52 - phosphoserine transaminase and Organism(s) Caenorhabditis elegans

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.52 phosphoserine transaminase
IUBMB Comments
A pyridoxal 5'-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli . Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis . Non-phosphorylated forms of serine and threonine are not substrates . The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine .
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Caenorhabditis elegans
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
Synonyms
psat, phosphoserine aminotransferase, phosphoserine aminotransferase 1, ehpsat, 3-phosphoserine aminotransferase, psat2, l-phosphoserine aminotransferase, psat beta, bmpsat, psat alpha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoserine aminotransferase
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hydroxypyruvic phosphate-glutamic transaminase
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L-phosphoserine aminotransferase
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phosphohydroxypyruvate transaminase
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phosphohydroxypyruvic-glutamic transaminase
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phosphoserine aminotransferase
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PSAT
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-serine:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli [3]. Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4]. The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-90-4
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SERC_CAEEL
370
0
41002
Swiss-Prot
other Location (Reliability: 3)